Identification in Marinomonas mediterranea of a novel quinoprotein with glycine oxidase activity
Article first published online: 22 JUL 2013
© 2013 The Authors. Microbiology Open published by John Wiley & Sons Ltd.
This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
Volume 2, Issue 4, pages 684–694, August 2013
How to Cite
MicrobiologyOpen 2013; 2(4): 684–694
- Issue published online: 12 AUG 2013
- Article first published online: 22 JUL 2013
- Manuscript Accepted: 7 JUN 2013
- Manuscript Revised: 29 MAY 2013
- Manuscript Received: 15 APR 2013
- Ministerio de Ciencia e Innovación. Grant Numbers: BIO2010-15226, 11867/PI/09
- European Commission
- Glycine oxidase;
- hydrogen peroxide;
- Marinomonas mediterranea ;
A novel enzyme with lysine-epsilon oxidase activity was previously described in the marine bacterium Marinomonas mediterranea. This enzyme differs from other l-amino acid oxidases in not being a flavoprotein but containing a quinone cofactor. It is encoded by an operon with two genes lodA and lodB. The first one codes for the oxidase, while the second one encodes a protein required for the expression of the former. Genome sequencing of M. mediterranea has revealed that it contains two additional operons encoding proteins with sequence similarity to LodA. In this study, it is shown that the product of one of such genes, Marme_1655, encodes a protein with glycine oxidase activity. This activity shows important differences in terms of substrate range and sensitivity to inhibitors to other glycine oxidases previously described which are flavoproteins synthesized by Bacillus. The results presented in this study indicate that the products of the genes with different degrees of similarity to lodA detected in bacterial genomes could constitute a reservoir of different oxidases.